Recent advances in technology have allowed for large scale genomic characterisation of a number of organisms, including most recently man. While this information is unquestionally valuable in the efforts to understand biological and patho-biological mechanisms, it has also been recognized that a deeper understanding of these mechanisms will rely in a more systematic analysis of the products of genetic information, namely proteins. In the middle of the 1990’s the term `proteomics` was coined to designate a new approach in life sciences with the goal to characterize the full complement of proteins within a cell, tissue or even an organism.
The most commonly used approach in proteomics research is the combination of two-dimensional gel electrophoresis (2-DE) for separation and quantitative image analysis with the micro-scale identification of the proteins using mass spectrometry. Due to the limitations of 2-DE, including the failure to detect low abundant proteins, several new technologies have been developed. A central idea is to understand the great complexity of the proteome. Prefractionation using affinity-purification prior to 2-DE or use of protein chips with selective binding surfaces or immobilized antibodies provide for the reduction of complexity that is necessary for accurate protein profiling. Multi-dimensional HPLC or capillary isoelectric focusing in combination with mass spectrometry is now able to resolve and identify rapidly up to 1000 proteins and by the use of different stable-isotope affinity tags (ICAT technology) quantify protein levels.
But simple profiling of proteins does not describe the function of the proteins within a cell and modern proteomics research will also concentrate on post translational modifications and protein-protein interactions. When recognized within the limits of the currently available technology, proteomics will become an invaluable tool for the understanding of biological and patho-biological relationships.
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